Therapeutic targeting of TEAD transcription factors in cancer

Oncogenic Signaling Pathways in The Cancer Genome Atlas

Sanchez-Vega, F., Mina, M., Armenia, J., Chatila, W. K., Luna, A., La, K. C., Dimitriadoy, S., Liu, D. L., Kantheti, H. S., Saghafinia, S., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.035 · Cited by 3,201 · see citing works

TEAD mediates YAP-dependent gene induction and growth control

Zhao, B., Ye, X., Yu, J., Li, L., Li, W., Li, S., Yu, J., Lin, J. D., Wang, C.-Y., Chinnaiyan, A. M., et al. (2008) · Genes & Development · doi:10.1101/gad.1664408 · Cited by 2,498 · see citing works

YAP/TAZ at the Roots of Cancer

Zanconato, F., Cordenonsi, M., & Piccolo, S. (2016) · Cancer Cell · doi:10.1016/j.ccell.2016.05.005 · Cited by 1,970 · see citing works

The Hippo pathway and human cancer

Harvey, K. F., Zhang, X., & Thomas, D. M. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3458 · Cited by 1,852 · see citing works

Regulation of the Hippo-YAP Pathway by G-Protein-Coupled Receptor Signaling

Yu, F.-X., Zhao, B., Panupinthu, N., Jewell, J. L., Lian, I., Wang, L. H., Zhao, J., Yuan, H., Tumaneng, K., Li, H., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.037 · Cited by 1,628 · see citing works

Genetic and pharmacological disruption of the TEAD–YAP complex suppresses the oncogenic activity of YAP

Liu-Chittenden, Y., Huang, B., Shim, J. S., Chen, Q., Lee, S.-J., Anders, R. A., Liu, J. O., & Pan, D. (2012) · Genes & Development · doi:10.1101/gad.192856.112 · Cited by 1,452 · see citing works

The Hippo Pathway: Biology and Pathophysiology

Ma, S., Meng, Z., Chen, R., & Guan, K.-L. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-111829 · Cited by 1,387 · see citing works

Genome-wide association between YAP/TAZ/TEAD and AP-1 at enhancers drives oncogenic growth

Zanconato, F., Forcato, M., Battilana, G., Azzolin, L., Quaranta, E., Bodega, B., Rosato, A., Bicciato, S., Cordenonsi, M., & Piccolo, S. (2015) · Nature Cell Biology · doi:10.1038/ncb3216 · Cited by 1,219 · see citing works

YAP/TAZ upstream signals and downstream responses

Totaro, A., Panciera, T., & Piccolo, S. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0142-z · Cited by 1,086 · see citing works

Hippo–YAP/TAZ signalling in organ regeneration and regenerative medicine

Moya, I. M., & Halder, G. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0086-y · Cited by 981 · see citing works

Comprehensive genomic analysis of malignant pleural mesothelioma identifies recurrent mutations, gene fusions and splicing alterations

Bueno, R., Stawiski, E. W., Goldstein, L. D., Durinck, S., Rienzo, A. D., Modrusan, Z. D., Gnad, F., Nguyen, T. T., Jaiswal, B. S., Chirieac, L. R., et al. (2016) · Nature Genetics · doi:10.1038/ng.3520 · Cited by 920 · see citing works

The Hippo Signaling Pathway in Development and Disease

Zheng, Y., & Pan, D. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.06.003 · Cited by 867 · see citing works

Targeting the Hippo pathway in cancer, fibrosis, wound healing and regenerative medicine

Dey, A., Varelas, X., & Guan, K.-L. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0070-z · Cited by 860 · see citing works

TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm

Vassilev, A., Kaneko, K. J., Shu, H., Zhao, Y., & DePamphilis, M. L. (2001) · Genes & Development · doi:10.1101/gad.888601 · Cited by 719 · see citing works

E-cadherin mediates contact inhibition of proliferation through Hippo signaling-pathway components

Kim, N.-G., Koh, E., Chen, X., & Gumbiner, B. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103345108 · Cited by 698 · see citing works

The TEAD/TEF Family Protein Scalloped Mediates Transcriptional Output of the Hippo Growth-Regulatory Pathway

Wu, S., Liu, Y., Zheng, Y., Dong, J., & Pan, D. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.01.007 · Cited by 640 · see citing works

Hippo-Independent Activation of YAP by the GNAQ Uveal Melanoma Oncogene through a Trio-Regulated Rho GTPase Signaling Circuitry

Feng, X., Degese, M. S., Iglesias‐Bartolomé, R., Vaque, J. P., Molinolo, A., Rodrigues, M. W., Zaidi, M. R., Ksander, B. R., Merlino, G. T., Sodhi, A., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.04.016 · Cited by 559 · see citing works

The Hippo effector YAP promotes resistance to RAF- and MEK-targeted cancer therapies

Lin, L., Sabnis, A. J., Chan, E., Olivas, V., Cade, L., Pazarentzos, E., Asthana, S., Neel, D., Yan, J. J., Lu, X., et al. (2015) · Nature Genetics · doi:10.1038/ng.3218 · Cited by 551 · see citing works

Comprehensive Molecular Characterization of the Hippo Signaling Pathway in Cancer

Wang, Y., Xu, X., Maglic, D., Dill, M. T., Mojumdar, K., Ng, P. K.-S., Jeong, K. J., Tsang, Y. H., Moreno, D., Bhavana, V. H., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.10.001 · Cited by 500 · see citing works

Treatment-Induced Tumor Dormancy through YAP-Mediated Transcriptional Reprogramming of the Apoptotic Pathway

Kurppa, K. J., Liu, Y., To, C., Zhang, T., Fan, M., Vajdi, A., Knelson, E. H., Xie, Y., Lim, K., Cejas, P., et al. (2020) · Cancer Cell · doi:10.1016/j.ccell.2019.12.006 · Cited by 475 · see citing works

Mutant Gq/11 Promote Uveal Melanoma Tumorigenesis by Activating YAP

Yu, F., Luo, J., Mo, J., Liu, G., Kim, Y. C., Meng, Z., Zhao, L., Peyman, G. A., Ouyang, H. W., Jiang, W., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.04.017 · Cited by 464 · see citing works

Role of Merlin/NF2 inactivation in tumor biology

Petrilli, A. M., & Fernández‐Valle, C. (2015) · Oncogene · doi:10.1038/onc.2015.125 · Cited by 459 · see citing works

SCALLOPED Interacts with YORKIE, the Nuclear Effector of the Hippo Tumor-Suppressor Pathway in Drosophila

Goulev, Y., Fauny, J., Gonzalez-Marti, B., Flagiello, D., Silber, J., & Zider, A. (2008) · Current Biology · doi:10.1016/j.cub.2008.02.034 · Cited by 452 · see citing works

YAP/TAZ Signaling and Resistance to Cancer Therapy

Nguyen, C. D. K., & Yi, C. (2019) · Trends in Cancer · doi:10.1016/j.trecan.2019.02.010 · Cited by 437 · see citing works

Hippo Pathway in Cancer: Aberrant Regulation and Therapeutic Opportunities

Calses, P. C., Crawford, J. J., Lill, J. R., & Dey, A. (2019) · Trends in cancer · doi:10.1016/j.trecan.2019.04.001 · Cited by 423 · see citing works

Structural insights into the YAP and TEAD complexPreprint

Li, Z., Zhao, B., Wang, P., Chen, F., Dong, Z., Yang, H., Guan, K., & Xu, Y. (2010) · Genes & Development · doi:10.1101/gad.1865810 · Cited by 406 · see citing works

Identification of a Disease-Defining Gene Fusion in Epithelioid Hemangioendothelioma

Tanas, M. R., Sboner, A., Oliveira, A. M., Erickson‐Johnson, M. R., Hespelt, J., Hanwright, P. J., Flanagan, J., Luo, Y., Fenwick, K., Natrajan, R., et al. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002409 · Cited by 399 · see citing works

The Hippo pathway in cancer: YAP/TAZ and TEAD as therapeutic targets in cancer

Cunningham, R., & Hansen, C. G. (2022) · Clinical Science · doi:10.1042/cs20201474 · Cited by 334 · see citing works

Transcriptional enhancer factor 1 disruption by a retroviral gene trap leads to heart defects and embryonic lethality in mice.Preprint

Chen, Z., Friedrich, G., & Soriano, P. M. (1994) · Genes & Development · doi:10.1101/gad.8.19.2293 · Cited by 332 · see citing works

Autopalmitoylation of TEAD proteins regulates transcriptional output of the Hippo pathway

Chan, P., Han, X., Zheng, B., DeRan, M., Yu, J., Jarugumilli, G. K., Deng, H., Pan, D., Luo, X., & Wu, X. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2036 · Cited by 313 · see citing works

Rescue of Hippo coactivator YAP1 triggers DNA damage–induced apoptosis in hematological cancers

Cottini, F., Hideshima, T., Xu, C., Sattler, M., Dori, M., Agnelli, L., ten Hacken, E., Bertilaccio, M. T. S., Antonini, E., Neri, A., et al. (2014) · Nature Medicine · doi:10.1038/nm.3562 · Cited by 310 · see citing works

YAP/TAZ: Drivers of Tumor Growth, Metastasis, and Resistance to Therapy

Thompson, B. J. (2020) · BioEssays · doi:10.1002/bies.201900162 · Cited by 262 · see citing works

Regulation of TEAD Transcription Factors in Cancer Biology

Huh, H., Kim, D., Jeong, H.-S., & Park, H. (2019) · Cells · doi:10.3390/cells8060600 · Cited by 259 · see citing works

Actin remodeling confers BRAF inhibitor resistance to melanoma cells through YAP/TAZ activation

Kim, M. H., Kim, J., Hong, H., Lee, J. J.-K., Lee, J., Jung, E., & Kim, J. (2015) · The EMBO Journal · doi:10.15252/embj.201592081 · Cited by 259 · see citing works

Emerging roles of TEAD transcription factors and its coactivators in cancers

Pobbati, A. V., & Hong, W. (2013) · Cancer Biology & Therapy · doi:10.4161/cbt.23788 · Cited by 256 · see citing works

Structural basis of YAP recognition by TEAD4 in the Hippo pathwayPreprint

Chen, L., Chan, S. W., Zhang, X., Walsh, M. A., Lim, C. J., Hong, W., & Song, H. (2010) · Genes & Development · doi:10.1101/gad.1865310 · Cited by 251 · see citing works

A combat with the YAP/TAZ-TEAD oncoproteins for cancer therapy

Pobbati, A. V., & Hong, W. (2020) · Theranostics · doi:10.7150/thno.40889 · Cited by 223 · see citing works

Targeting the Central Pocket in Human Transcription Factor TEAD as a Potential Cancer Therapeutic Strategy

Pobbati, A. V., Han, X. Y., Hung, A. W., Seetoh, W.-G., Huda, N., Chen, G.-Y., Kang, C., Chia, C. S. B., Luo, X., Hong, W., et al. (2015) · Structure · doi:10.1016/j.str.2015.09.009 · Cited by 212 · see citing works

Regulation of Hippo pathway transcription factor TEAD by p38 MAPK-induced cytoplasmic translocation

Lin, K. C., Moroishi, T., Meng, Z., Jeong, H.-S., Plouffe, S. W., Sekido, Y., Han, J., Park, H. W., & Guan, K. (2017) · Nature Cell Biology · doi:10.1038/ncb3581 · Cited by 205 · see citing works

Tumor-selective proteotoxicity of verteporfin inhibits colon cancer progression independently of YAP1

Zhang, H., Ramakrishnan, S. K., Triner, D., Centofanti, B., Maitra, D., Győrffy, B., Sebolt-Leopold, J. S., Dame, M. K., Varani, J., Brenner, D. E., et al. (2015) · Science Signaling · doi:10.1126/scisignal.aac5418 · Cited by 196 · see citing works

Binary pan-cancer classes with distinct vulnerabilities defined by pro- or anti-cancer YAP/TEAD activity

Pearson, J. D., Huang, K., Pacal, M., McCurdy, S. R., Lü, S., Aubry, A., Yu, T., Wadosky, K. M., Zhang, L., Wang, T., et al. (2021) · Cancer Cell · doi:10.1016/j.ccell.2021.06.016 · Cited by 172 · see citing works

Structural and Functional Similarity between the Vgll1-TEAD and the YAP-TEAD Complexes

Pobbati, A. V., Chan, S. W., Lee, I., Song, H., & Hong, W. (2012) · Structure · doi:10.1016/j.str.2012.04.004 · Cited by 171 · see citing works

VGLL4 targets a TCF4–TEAD4 complex to coregulate Wnt and Hippo signalling in colorectal cancer

Jiao, S., Li, C., Qian, H., Miao, H., Zhang, L., Li, L., & Zhou, Z. (2017) · Nature Communications · doi:10.1038/ncomms14058 · Cited by 157 · see citing works

Crumbs3-Mediated Polarity Directs Airway Epithelial Cell Fate through the Hippo Pathway Effector Yap

Szymaniak, A. D., Mahoney, J. E., Cardoso, W. V., & Varelas, X. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.06.020 · Cited by 153 · see citing works

YAP1 and its fusion proteins in cancer initiation, progression and therapeutic resistance

Szulzewsky, F., Holland, E. C., & Vasioukhin, V. I. (2021) · Developmental Biology · doi:10.1016/j.ydbio.2020.12.018 · Cited by 153 · see citing works

TEAD4 ensures postimplantation development by promoting trophoblast self-renewal: An implication in early human pregnancy loss

Saha, B., Ganguly, A., Home, P., Bhattacharya, B., Ray, S. S., Ghosh, A., Rumi, M. A. K., Marsh, C. A., French, V. A., Gunewardena, S., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2002449117 · Cited by 153 · see citing works

Transcriptional repression of estrogen receptor alpha by YAP reveals the Hippo pathway as therapeutic target for ER+ breast cancer

Ma, S., Tang, T. T.-L., Probst, G. D., Konradi, A. W., Jin, C., Li, F., Gutkind, J. S., Fu, X., & Guan, K. (2022) · Nature Communications · doi:10.1038/s41467-022-28691-0 · Cited by 145 · see citing works

Pharmacological blockade of TEAD–YAP reveals its therapeutic limitation in cancer cells

Sun, Y., Hu, L., Tao, Z., Jarugumilli, G. K., Erb, H., Singh, A., Li, Q., Cotton, J. L., Greninger, P., Egan, R. K., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34559-0 · Cited by 145 · see citing works

Epiblast Formation by TEAD-YAP-Dependent Expression of Pluripotency Factors and Competitive Elimination of Unspecified Cells

Hashimoto, M., & Sasaki, H. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.05.024 · Cited by 140 · see citing works

The novel potent TEAD inhibitor, K-975, inhibits YAP1/TAZ-TEAD protein-protein interactions and exerts an anti-tumor effect on malignant pleural mesothelioma.

Kaneda, A., Seike, T., Danjo, T., Nakajima, T., Otsubo, N., Yamaguchi, D., Tsuji, Y., Hamaguchi, K., Yasunaga, M., Nishiya, Y., et al. (2020) · PubMed Central · Cited by 139 · see citing works

Targeting intrinsically disordered proteins at the edge of chaos

Ruan, H., Sun, Q., Zhang, W., Liu, Y., & Lai, L. (2019) · Drug Discovery Today · doi:10.1016/j.drudis.2018.09.017 · Cited by 133 · see citing works

One cell‐specific and three ubiquitous nuclear proteins bind in vitro to overlapping motifs in the domain B1 of the SV40 enhancer.

Xiao, J. H., Davidson, I., Ferrandon, D., Rosales, R., Vigneron, M., Macchi, M., Ruffenach, F., & Chambon, P. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb02606.x · Cited by 122 · see citing works

TEAD family transcription factors in development and disease

Currey, L., Thor, S., & Piper, M. (2021) · Development · doi:10.1242/dev.196675 · Cited by 120 · see citing works

Mechanism of action of a WWTR1(TAZ)-CAMTA1 fusion oncoprotein

Tanas, M. R., Ma, S., Jadaan, F. O., Ng, C. K. Y., Weigelt, B., Reis-Filho, J. S., & Rubin, B. P. (2015) · Oncogene · doi:10.1038/onc.2015.148 · Cited by 113 · see citing works

Crystal structure of TAZ-TEAD complex reveals a distinct interaction mode from that of YAP-TEAD complex

Kaan, H. Y. K., Chan, S. W., Tan, S. K. J., Guo, F., Lim, C. J., Hong, W., & Song, H. (2017) · Scientific Reports · doi:10.1038/s41598-017-02219-9 · Cited by 111 · see citing works

Verteporfin exhibits YAP-independent anti-proliferative and cytotoxic effects in endometrial cancer cells

Dasari, V. R., Mazack, V., Feng, W., Nash, J. D., Carey, D. J., & Gogoi, R. P. (2017) · Oncotarget · doi:10.18632/oncotarget.15614 · Cited by 108 · see citing works

Glucocorticoid Receptor Signaling Activates TEAD4 to Promote Breast Cancer Progression

He, L., Yuan, L., Sun, Y., Wang, P., Zhang, H., Feng, X., Wang, Z., Zhang, W., Yang, C., Zeng, Y. A., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-0012 · Cited by 107 · see citing works

Focal adhesion kinase-YAP signaling axis drives drug-tolerant persister cells and residual disease in lung cancer

Haderk, F., Chou, Y., Čech, L., Fernández-Méndez, C., Yu, J. X., Olivas, V. R., Meraz, I. M., Rabago, D. B., Kerr, D. L., Gómez, C. F., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47423-0 · Cited by 106 · see citing works

MCAT Elements and the TEF-1 Family of Transcription Factors in Muscle Development and Disease

Yoshida, T. (2007) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.107.155788 · Cited by 104 · see citing works

YAP induces an oncogenic transcriptional program through TET1-mediated epigenetic remodeling in liver growth and tumorigenesis

Wu, B.-K., Mei, S.-C., Chen, E. H., Zheng, Y., & Pan, D. (2022) · Nature Genetics · doi:10.1038/s41588-022-01119-7 · Cited by 90 · see citing works

Comparison of tumor-associated YAP1 fusions identifies a recurrent set of functions critical for oncogenesisPreprint

Szulzewsky, F., Arora, S., Hoellerbauer, P., King, C., Nathan, E., Chan, M., Cimino, P. J., Ozawa, T., Kawauchi, D., Pajtler, K. W., et al. (2020) · Genes & Development · doi:10.1101/gad.338681.120 · Cited by 81 · see citing works

Discovery of drugs that directly target the intrinsically disordered region of the androgen receptor

Sadar, M. D. (2020) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2020.1732920 · Cited by 80 · see citing works

The Hippo Pathway as a Driver of Select Human Cancers

Kulkarni, A., Chang, M. T., Vissers, J. H. A., Dey, A., & Harvey, K. F. (2020) · Trends in cancer · doi:10.1016/j.trecan.2020.04.004 · Cited by 77 · see citing works

YAP inhibits ERα and ER+ breast cancer growth by disrupting a TEAD-ERα signaling axis

Li, X., Zhuo, S., Zhuang, T., Cho, Y. S., Wu, G., Liu, Y., Mu, K., Zhang, K., Su, P., Yang, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30831-5 · Cited by 77 · see citing works

Mammalian display screening of diverse cystine-dense peptides for difficult to drug targets

Crook, Z. R., Sevilla, G. P., Friend, D. J., Brusniak, M., Bandaranayake, A. D., Clarke, M., Gewe, M. M., Mhyre, A. J., Baker, D. A., Strong, R. K., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02098-8 · Cited by 77 · see citing works

Yes‐associated protein/TEA domain family member and hepatocyte nuclear factor 4‐alpha (HNF4α) repress reciprocally to regulate hepatocarcinogenesis in rats and mice

Cai, W., Lin, L., Hao, H., Zhang, S., Ma, F., Hong, X., Zhang, H., Liu, Q., Ye, G., Sun, G., et al. (2016) · Hepatology · doi:10.1002/hep.28911 · Cited by 76 · see citing works

Update on biology and management of mesothelioma

Asciak, R., George, V., & Rahman, N. M. (2021) · European Respiratory Review · doi:10.1183/16000617.0226-2020 · Cited by 75 · see citing works

Recent Therapeutic Approaches to Modulate the Hippo Pathway in Oncology and Regenerative Medicine

Barry, E., Simov, V., Valtingojer, I., & Venier, O. (2021) · Cells · doi:10.3390/cells10102715 · Cited by 71 · see citing works

Effect of the acylation of TEAD4 on its interaction with co‐activators YAP and TAZ

Mesrouze, Y., Meyerhofer, M., Bokhovchuk, F. M., Fontana, P., Zimmermann, C., Martin, T., Delaunay, C., Izaac, A., Kallen, J. A., Schmelzle, T., et al. (2017) · Protein Science · doi:10.1002/pro.3312 · Cited by 70 · see citing works

Covalent disruptor of YAP-TEAD association suppresses defective Hippo signaling

Fan, M., Lu, W., Che, J., Kwiatkowski, N. P., Gao, Y., Seo, H.-S., Ficarro, S. B., Gokhale, P. C., Liu, Y., Geffken, E. A., et al. (2022) · eLife · doi:10.7554/elife.78810 · Cited by 68 · see citing works

YAP1 Mediates Resistance to MEK1/2 Inhibition in Neuroblastomas with Hyperactivated RAS Signaling

Coggins, G. E., Farrel, A., Rathi, K. S., Hayes, C. M., Scolaro, L., Rokita, J. L., & Maris, J. M. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-1415 · Cited by 66 · see citing works

WWTR1(TAZ)-CAMTA1 gene fusion is sufficient to dysregulate YAP/TAZ signaling and drive epithelioid hemangioendothelioma tumorigenesisPreprint

Seavey, C. N., Pobbati, A. V., Hallett, A., Ma, S., REYNOLDS, J. P., Kanai, R., Lamar, J. M., & Rubin, B. P. (2021) · Genes & Development · doi:10.1101/gad.348220.120 · Cited by 66 · see citing works

Machine-Learning and Chemicogenomics Approach Defines and Predicts Cross-Talk of Hippo and MAPK Pathways

Pham, T. H., Hagenbeek, T. J., Lee, H.-J., Li, J., Rose, C. M., Lin, E., Yu, M., Martin, S. E., Piskol, R., Lacap, J. A., et al. (2021) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-0706 · Cited by 64 · see citing works

Inhibition of YAP/TAZ-driven TEAD activity prevents growth of NF2-null schwannoma and meningioma

Laraba, L., Hillson, L., de Guibert, J. G., Hewitt, A., Jaques, M. R., Tang, T. T.-L., Post, L. E., Ercolano, E., Rai, G., Yang, S., et al. (2022) · Brain · doi:10.1093/brain/awac342 · Cited by 63 · see citing works

TEAD4 overexpression promotes epithelial-mesenchymal transition and associates with aggressiveness and adverse prognosis in head neck squamous cell carcinoma

Zhang, W., Li, J., Wu, Y., Ge, H., Song, Y., Wang, D., Yuan, H., Jiang, H., Wang, Y., & Cheng, J. (2018) · Cancer Cell International · doi:10.1186/s12935-018-0675-z · Cited by 55 · see citing works

CRB3 regulates contact inhibition by activating the Hippo pathway in mammary epithelial cells

Mao, X., Li, P., Wang, Y., Liang, Z., Liu, J., Li, J., Jiang, Y., Bao, G., Li, L., Zhu, B., et al. (2017) · Cell Death and Disease · doi:10.1038/cddis.2016.478 · Cited by 52 · see citing works

Protein-Protein Interaction Disruptors of the YAP/TAZ-TEAD Transcriptional Complex

Pobbati, A. V., & Rubin, B. P. (2020) · Molecules · doi:10.3390/molecules25246001 · Cited by 52 · see citing works

Progress with YAP/TAZ-TEAD inhibitors: a patent review (2018-present)

Zagiel, B., Melnyk, P., & Cotelle, P. (2022) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2022.2096436 · Cited by 51 · see citing works

Regulatory enhancer profiling of mesenchymal-type gastric cancer reveals subtype-specific epigenomic landscapes and targetable vulnerabilities

Ho, S. W. T., Sheng, T., Xing, M., Ooi, W. F., Xu, C., Sundar, R., Huang, K. K., Li, Z., Kumar, V., Ramnarayanan, K., et al. (2022) · Gut · doi:10.1136/gutjnl-2021-326483 · Cited by 51 · see citing works

Structure-based design of potent linear peptide inhibitors of the YAP-TEAD protein-protein interaction derived from the YAP omega-loop sequence

Furet, P., Salem, B., Mesrouze, Y., Schmelzle, T., Lewis, I., Kallen, J. A., & Chêne, P. (2019) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2019.06.022 · Cited by 49 · see citing works

Both YAP1-MAML2 and constitutively active YAP1 drive the formation of tumors that resemble NF2 mutant meningiomas in micePreprint

Szulzewsky, F., Arora, S., Arakaki, A. K. S., Sievers, P., Bonnin, D. A. A., Paddison, P. J., Sahm, F., Cimino, P. J., Gujral, T. S., & Holland, E. C. (2022) · Genes & Development · doi:10.1101/gad.349876.122 · Cited by 46 · see citing works

The First Class of Small Molecules Potently Disrupting the YAP‐TEAD Interaction by Direct Competition

Furet, P., Bordas, V., Douget, M. L., Salem, B., Mesrouze, Y., Imbach, P. A., Sellner, H., Voegtle, M., Soldermann, N., Chapeau, E. A., et al. (2022) · ChemMedChem · doi:10.1002/cmdc.202200303 · Cited by 45 · see citing works

Structural and ligand-binding analysis of the YAP-binding domain of transcription factor TEAD4

Li, Y., Liu, S., Ng, E. Y., Li, R., Poulsen, A., Hill, J., Pobbati, A. V., Hung, A. W., Hong, W., Keller, T. H., et al. (2018) · Biochemical Journal · doi:10.1042/bcj20180225 · Cited by 43 · see citing works

The TEA domain family transcription factor TEAD4 represses murine adipogenesis by recruiting the cofactors VGLL4 and CtBP2 into a transcriptional complex

Zhang, W., Xu, J., Li, J., Guo, T., Jiang, D., Feng, X., Ma, X., He, L., Wu, W., Yin, M.-X., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003608 · Cited by 43 · see citing works

Discovery of a cryptic site at the interface 2 of TEAD – Towards a new family of YAP/TAZ-TEAD inhibitors

Sturbaut, M., Bailly, F., Coevoet, M., Sileo, P., Pugnière, M., Liberelle, M., Magnez, R., Thuru, X., Chartier‐Harlin, M., Melnyk, P., et al. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113835 · Cited by 42 · see citing works

TEAD4 promotes colorectal tumorigenesis via transcriptionally targeting YAP1

Tang, J., Yu, C.-Y., Bao, Y.-J., Lu, C., Chen, J., Yang, S.-L., Chen, H., Hong, J., & Fang, J. (2017) · Cell Cycle · doi:10.1080/15384101.2017.1403687 · Cited by 41 · see citing works

Identification of FAM181A and FAM181B as new interactors with the TEAD transcription factors

Bokhovchuk, F. M., Mesrouze, Y., Delaunay, C., Martin, T., Villard, F., Meyerhofer, M., Fontana, P., Zimmermann, C., Erdmann, D., Furet, P., et al. (2019) · Protein Science · doi:10.1002/pro.3775 · Cited by 37 · see citing works

Hot Spot Analysis of YAP-TEAD Protein-Protein Interaction Using the Fragment Molecular Orbital Method and Its Application for Inhibitor Discovery

Kim, J., Lim, H., Moon, S., Cho, S. Y., Kim, M., Park, J. H., Park, H. W., & No, K. T. (2021) · Cancers · doi:10.3390/cancers13164246 · Cited by 37 · see citing works

Inhibitors of the Hippo Pathway Kinases STK3/MST2 and STK4/MST1 Have Utility for the Treatment of Acute Myeloid Leukemia

Bata, N., Chaikuad, A., Bakas, N. A., Limpert, A. S., Lambert, L. J., Sheffler, D. J., Berger, L. M., Liu, G., Yuan, C., Wang, L., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00804 · Cited by 36 · see citing works

Cell adhesion molecule KIRREL1 is a feedback regulator of Hippo signaling recruiting SAV1 to cell-cell contact sites

Paul, A., Annunziato, S., Lu, B., Sun, T., Evrova, O., Planas‐Paz, L., Orsini, V., Terracciano, L., Charlat, O., Yang, Z., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28567-3 · Cited by 35 · see citing works

Common Secondary Genomic Variants Associated With Advanced Epithelioid Hemangioendothelioma

Seligson, N. D., Awasthi, A., Millis, S. Z., Turpin, B. K., Meyer, C. F., Grand’Maison, A., Liebner, D. A., Hays, J. L., & Chen, J. L. (2019) · JAMA Network Open · doi:10.1001/jamanetworkopen.2019.12416 · Cited by 32 · see citing works

The Surprising Features of the TEAD4‐Vgll1 Protein–Protein Interaction

Mesrouze, Y., Hau, J. C., Erdmann, D., Zimmermann, C., Fontana, P., Schmelzle, T., & Chêne, P. (2014) · ChemBioChem · doi:10.1002/cbic.201300715 · Cited by 30 · see citing works

Nerfin-1 represses transcriptional output of Hippo signaling in cell competition

Guo, P., Lee, C.-H., Lei, H., Zheng, Y., Prieto, K. D. P., & Pan, D. (2019) · eLife · doi:10.7554/elife.38843 · Cited by 29 · see citing works

Homeobox A4 suppresses vascular remodeling by repressing YAP/TEAD transcriptional activity

Kimura, M., Horie, T., Baba, O., Ide, Y., Tsuji, S., Rodriguez, R. R., Watanabe, T., Yamasaki, T., Otani, C., Xu, S., et al. (2020) · EMBO Reports · doi:10.15252/embr.201948389 · Cited by 29 · see citing works

TEA Domain Transcription Factor 4 Is the Major Mediator of Yes-Associated Protein Oncogenic Activity in Mouse and Human Hepatoblastoma

Zhang, J., Pin, L., Tao, J., Wang, P., Zhang, Y., Song, X., Che, L., Sumazin, P., Ribback, S., Kiss, A., et al. (2019) · American Journal Of Pathology · doi:10.1016/j.ajpath.2019.01.016 · Cited by 28 · see citing works

Toward the Design of Ligands Selective for the C-Terminal Domain of TEADs

Liberelle, M., Toulotte, F., Renault, N., Gelin, M., Allemand, F., Melnyk, P., Guichou, J., & Cotelle, P. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00075 · Cited by 23 · see citing works

Pan-cancer analysis, cell and animal experiments revealing TEAD4 as a tumor promoter in ccRCC

Li, F., Feng, Y., Jiang, Q., Zhang, J., Wu, F., Li, Q., Jing, X., Wang, X., & Huang, C. Y. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.120327 · Cited by 23 · see citing works

Loss of CDKN2A Cooperates with WWTR1(TAZ)–CAMTA1 Gene Fusion to Promote Tumor Progression in Epithelioid Hemangioendothelioma

Seavey, C. N., Hallett, A., Li, S., Che, K., Pobbati, A. V., Ma, S., Burtscher, A., Kanai, R., Lamar, J. M., & Rubin, B. P. (2023) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-22-2497 · Cited by 23 · see citing works

An Early Association between the α-Helix of the TEAD Binding Domain of YAP and TEAD Drives the Formation of the YAP:TEAD Complex

Bokhovchuk, F. M., Mesrouze, Y., Meyerhofer, M., Zimmermann, C., Fontana, P., Erdmann, D., Jemth, P., & Chêne, P. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00217 · Cited by 22 · see citing works

Association of subcellular localization of TEAD transcription factors with outcome and progression in pancreatic ductal adenocarcinoma

Drexler, R., Fahy, R., Küchler, M., Wagner, K. C., Reese, T., Ehmke, M., Feyerabend, B., Kleine, M., & Oldhafer, K. J. (2020) · Pancreatology · doi:10.1016/j.pan.2020.12.003 · Cited by 22 · see citing works

Abstract 5364: The TEAD autopalmitoylation inhibitor VT3989 improves efficacy and increases durability of efficacy of osimertinib in preclinical EGFR mutant tumor models

Tang, T. T., & Post, L. E. (2022) · Cancer Research · doi:10.1158/1538-7445.am2022-5364 · Cited by 21 · see citing works

YAP1 is essential for malignant mesothelioma tumor maintenance

Calvet, L., Dos-Santos, O., Spanakis, E., Jean‐Baptiste, V., Bail, J.-C. L., Buzy, A., Paul, P., Henry, C., Valence, S., Dib, C., et al. (2022) · BMC Cancer · doi:10.1186/s12885-022-09686-y · Cited by 20 · see citing works

A focal adhesion kinase-YAP signaling axis drives drug tolerant persister cells and residual disease in lung cancerPreprint

Haderk, F., Fernández-Méndez, C., Čech, L., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.23.465573 · Cited by 18 · see citing works

Abstract 2156: IK-930 is a novel TEAD inhibitor for the treatment of cancers harboring mutations in the Hippo signal transduction pathway

Amidon, B., Sánchez-Martín, M., Bartolini, W. P., Syed, S., McGovern, K., Xu, L., Ecsedy, J., Zhang, X. M., Constan, A., & Castro, A. C. (2022) · Cancer Research · doi:10.1158/1538-7445.am2022-2156 · Cited by 18 · see citing works

The role of lysine palmitoylation/myristoylation in the function of the TEAD transcription factors

Mesrouze, Y., Aguilar, G., Meyerhofer, M., Bokhovchuk, F. M., Zimmermann, C., Fontana, P., Vissières, A., Voshol, H., Erdmann, D., Affolter, M., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-09127-7 · Cited by 15 · see citing works

TEADs serve as potential prognostic biomarkers and targets for human gastric cancer

Wang, M.-H., Li, B., Chen, Y., & Wang, J. (2022) · BMC Gastroenterology · doi:10.1186/s12876-022-02386-8 · Cited by 12 · see citing works

Aurintricarboxylic acid is a canonical disruptor of the TAZ-TEAD transcriptional complex

Che, K., Pobbati, A. V., Seavey, C. N., Federov, Y., Komar, A. A., Burtscher, A., Ma, S., & Rubin, B. P. (2022) · PLoS ONE · doi:10.1371/journal.pone.0266143 · Cited by 7 · see citing works

Direct and selective pharmacological disruption of the YAP–TEAD interface by IAG933 inhibits Hippo-dependent and RAS–MAPK-altered cancers

Chapeau, E. A., Sansregret, L., Galli, G. G., Chêne, P., Wartmann, M., Mourikis, T. P., Jaaks, P., Baltschukat, S., Barbosa, I. A. M., Bauer, D., et al. (2024) · Nature Cancer · doi:10.1038/s43018-024-00754-9 · Cited by 163 · see citing works

Genome-Wide CRISPR Screens Identify Multiple Synthetic Lethal Targets That Enhance KRASG12C Inhibitor Efficacy

Mukhopadhyay, S., Huang, H.-Y., Lin, Z., Ranieri, M., Li, S., Sahu, S., Liu, Y., Ban, Y., Guidry, K., Hu, H., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-23-2729 · Cited by 105 · see citing works

Expected and unexpected effects after systemic inhibition of Hippo transcriptional output in cancer

Baroja, I., Kyriakidis, N. C., Halder, G. A., & Moya, I. M. (2024) · Nature Communications · doi:10.1038/s41467-024-46531-1 · Cited by 92 · see citing works

TEAD Inhibition Overcomes YAP1/TAZ-Driven Primary and Acquired Resistance to KRASG12C Inhibitors

Edwards, A. C., Stalnecker, C. A., Jean Morales, A., Taylor, K. E., Klomp, J. E., Klomp, J. A., Waters, A. M., Sudhakar, N., Hallin, J., Tang, T. T., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-23-2994 · Cited by 91 · see citing works

New insights into the ambivalent role of YAP/TAZ in human cancers

Luo, J., Deng, L., Zou, H., Guo, Y., Tong, T., Huang, M., Ling, G., & Li, P. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02704-2 · Cited by 83 · see citing works

Targeting the Hippo pathway in cancer

Harvey, K. F., & Tang, T. T.-L. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-025-01234-0 · Cited by 65 · see citing works

Plastic persisters: revival stem cells in colorectal cancer

Tape, C. J. (2023) · Trends in cancer · doi:10.1016/j.trecan.2023.11.003 · Cited by 58 · see citing works

Hippo Signaling at the Hallmarks of Cancer and Drug Resistance

Kumar, R., & Hong, W. (2024) · Cells · doi:10.3390/cells13070564 · Cited by 47 · see citing works

The Hippo pathway: Organ size control and beyond

Guo, P., Wan, S., & Guan, K. (2024) · Pharmacological Reviews · doi:10.1016/j.pharmr.2024.100031 · Cited by 45 · see citing works

Pancreatic cancer: molecular pathogenesis and emerging therapeutic strategies

Rozengurt, E., & Eibl, G. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02499-y · Cited by 47 · see citing works

Cell softness renders cytotoxic T lymphocytes and T leukemic cells resistant to perforin-mediated killing

Zhou, Y., Wang, D., Zhou, L., Zhou, N., Wang, Z., Chen, J., Pang, R., Fu, H., Huang, Q., Dong, F., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45750-w · Cited by 41 · see citing works

Complex roles of Hippo-YAP/TAZ signaling in hepatocellular carcinoma

Shi, H., Zou, Y., Zhong, W., Li, Z., Wang, X., Yin, Y., Li, D., Liu, Y., & Li, M. (2023) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-023-05272-2 · Cited by 37 · see citing works

Cooperation between the Hippo and MAPK pathway activation drives acquired resistance to TEAD inhibition

Paul, S., Hagenbeek, T. J., Tremblay, J., Kameswaran, V., Ong, C. C., Liu, C., Guarnaccia, A. D., Mondo, J. A., Hsu, P., Kljavin, N. M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-56634-y · Cited by 31 · see citing works

Nuclear Import and Export of YAP and TAZ

Kofler, M., & Kapùs, A. (2023) · Cancers · doi:10.3390/cancers15204956 · Cited by 29 · see citing works

Targeting the Hippo pathway in cancer: kidney toxicity as a class effect of TEAD inhibitors?

Paul, S., Sims, J., Pham, T., & Dey, A. (2024) · Trends in cancer · doi:10.1016/j.trecan.2024.10.004 · Cited by 30 · see citing works

It’s all downstream from here: RTK/Raf/MEK/ERK pathway resistance mechanisms in glioblastoma

Yakubov, R., Kaloti, R., Persaud, P., McCracken, A., Zadeh, G. M., & Bunda, S. (2025) · Journal of Neuro-Oncology · doi:10.1007/s11060-024-04930-w · Cited by 28 · see citing works

Leveraging Hot Spots of TEAD–Coregulator Interactions in the Design of Direct Small Molecule Protein-Protein Interaction Disruptors Targeting Hippo Pathway Signaling

Zhao, B., Pobbati, A. V., Rubin, B. P., & Stauffer, S. R. (2023) · Pharmaceuticals · doi:10.3390/ph16040583 · Cited by 25 · see citing works

Mechanical Properties of Glioblastoma: Perspectives for YAP/TAZ Signaling Pathway and Beyond

Pontes, B., & Mendes, F. A. (2023) · Diseases · doi:10.3390/diseases11020086 · Cited by 26 · see citing works

A Single-Arm Phase 2 Trial of Trametinib in Patients with Locally Advanced or Metastatic Epithelioid Hemangioendothelioma

Schuetze, S. M., Ballman, K. V., Heise, R. S., Ganjoo, K. N., Davis, E. J., George, S., Burgess, M. A., Choy, E., Shepard, D. R., Tinoco, G., et al. (2024) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-23-3817 · Cited by 24 · see citing works

Palmitoylation: an emerging therapeutic target bridging physiology and disease

Li, W., Shen, J. M., Zhuang, A., Wang, R., Li, Q., Rabata, A., Zhang, Y., & Cao, D. (2025) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-025-00776-w · Cited by 24 · see citing works

Tyrosine phosphorylation-mediated YAP1-TFAP2A interactions coordinate transcription and trastuzumab resistance in HER2+ breast cancer

Zou, H., Luo, J., Guo, Y., Deng, L., Zeng, L., Pan, Y., & Li, P. (2024) · Drug Resistance Updates · doi:10.1016/j.drup.2024.101051 · Cited by 24 · see citing works

Design, Synthesis, and Bioevaluation of Transcriptional Enhanced Assocciated Domain (TEAD) PROTAC Degraders

Li, H., Ge, Z., Lin, K., He, W., Chu, Q., Zheng, M., Zhang, S., & Xu, T. (2024) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.4c00029 · Cited by 23 · see citing works

Pharmacological regulators of Hippo pathway: Advances and challenges of drug development

Lao, Z., Chen, X., Pan, B., Fang, B., Yang, W., & Qian, Y. (2025) · The FASEB Journal · doi:10.1096/fj.202401895rr · Cited by 21 · see citing works

Estrogen receptor activation remodels TEAD1 gene expression to alleviate hepatic steatosis

Sommerauer, C., Gallardo-Dodd, C. J., Savva, C., Hases, L., Birgersson, M., Indukuri, R., Shen, J. X., Carravilla, P., Geng, K., Søndergaard, J. N., et al. (2024) · Molecular Systems Biology · doi:10.1038/s44320-024-00024-x · Cited by 21 · see citing works

Hippo signaling in acute kidney injury to chronic kidney disease transition: Current understandings and future targets

Habshi, T., Shelke, V., Kale, A., Lech, M., & Gaikwad, A. B. (2023) · Drug Discovery Today · doi:10.1016/j.drudis.2023.103649 · Cited by 20 · see citing works

Nuclear deformation regulates YAP dynamics in cancer associated fibroblasts

Emon, B., Joy, M. S. H., Lalonde, L., Ghrayeb, A., Doha, U., Ladehoff, L. C., Brockstein, R., Saengow, C., Ewoldt, R. H., & Saif, M. T. A. (2023) · Acta Biomaterialia · doi:10.1016/j.actbio.2023.11.015 · Cited by 20 · see citing works

Deoxynivalenol regulates intestinal and stem cell regeneration via the Hippo pathway and clinical intervention strategies

Liao, P. (2025) · Toxicon · doi:10.1016/j.toxicon.2025.108553 · Cited by 18 · see citing works

TEAD-targeting small molecules induce a cofactor switch to regulate the Hippo pathway

Guarnaccia, A. D., Hagenbeek, T. J., Lee, W., Kljavin, N. M., Choi, M., Tombling, B. J., Peukert, C., Ulas, G., Kameswaran, V., Le, D., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2425984122 · Cited by 16 · see citing works

Endogenous YAP/TAZ partitioning in TEAD condensates orchestrates the Hippo response.

Zhu, T., Li, H., Mao, S., Zhu, Y., Cao, H.-Y., Zhang, Q., Zhen, N., Zhang, H.-X., Tian, Y., Guo, Y., et al. (2025) · Molecules and Cells · doi:10.1016/j.molcel.2025.08.014 · Cited by 19 · see citing works

Allosteric PROTACs: Expanding the Horizon of Targeted Protein Degradation

Frost, A. B., O’Connor, S., & Ciulli, A. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c14840 · Cited by 21 · see citing works

Development of HC-258, a Covalent Acrylamide TEAD Inhibitor That Reduces Gene Expression and Cell Migration

Fnaiche, A., Chan, H., Paquin, A., Suárez, N. G., Vu, V., Li, F., Allali‐Hassani, A., Cao, M. A., Szewczyk, M. M., Bolotokova, A., et al. (2023) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.3c00386 · Cited by 16 · see citing works

Identification of a Gene Signature That Predicts Dependence upon YAP/TAZ-TEAD

Kanai, R., Norton, E., Stern, P., Hynes, R. O., & Lamar, J. M. (2024) · Cancers · doi:10.3390/cancers16050852 · Cited by 16 · see citing works

Identification of resistance mechanisms to small-molecule inhibition of TEAD-regulated transcription

Kulkarni, A., Mohan, V., Tang, T. T.-L., Post, L. E., Chan, Y.-C., Manning, M., Thio, N., Parker, B. L., Dawson, M. A., Rosenbluh, J., et al. (2024) · EMBO Reports · doi:10.1038/s44319-024-00217-3 · Cited by 15 · see citing works

The recent advances and implications in cancer therapy for the hippo pathway

Chan, S. W., Ong, C., & Hong, W. (2025) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2025.102476 · Cited by 13 · see citing works

Development of LM-41 and AF-2112, two flufenamic acid-derived TEAD inhibitors obtained through the replacement of the trifluoromethyl group by aryl rings

Fnaiche, A., Mélin, L., Suárez, N. G., Paquin, A., Vu, V., Li, F., Allali‐Hassani, A., Bolotokova, A., Allemand, F., Gelin, M., et al. (2023) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2023.129488 · Cited by 13 · see citing works

The Hippo pathway in endometrial cancer: a potential therapeutic target?

Shen, X., Li, Q., Sun, Y., Chen, L., Xue, F., Tian, W., & Wang, Y. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1273345 · Cited by 13 · see citing works

VGLL2 and TEAD1 fusion proteins identified in human sarcoma drive YAP/TAZ-independent tumorigenesis by engaging EP300Preprint

Guo, S., Hu, X., Cotton, J. L., Ma, L., Li, Q., Cui, J., Wang, Y., Thakare, R., Tao, Z., Ip, Y. T., et al. (2024) · eLife · doi:10.7554/elife.98386 · Cited by 13 · see citing works

Reactivating Hippo by drug compounds to suppress gastric cancer and enhance chemotherapy sensitivity

Cao, Z., Hou, Y., Zhao, Z., Zhang, H., Tian, L., Zhang, Y., Dong, C., Guo, F., Tan, L., Han, Y., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107311 · Cited by 12 · see citing works

Direct Inhibition of the YAP : TEAD Interaction: An Unprecedented Drug Discovery Challenge

Chêne, P. (2024) · ChemMedChem · doi:10.1002/cmdc.202400361 · Cited by 12 · see citing works

ATXN3 deubiquitinates YAP1 to promote tumor growth.

Wang, S., Liu, K., Han, X., Cheng, Y., Zhao, E., Brat, D. J., Sun, Z., & Fang, D. (2023) · PubMed Central · Cited by 11 · see citing works

Exploring RNF213 in Ischemic Stroke and Moyamoya Disease: From Cellular Models to Clinical Insights

Tan, B. Y., Kok, C. H. P., Ng, M. B. J., Loong, S. S. E., Jou, E., Yeo, L. L. L., Han, W., Anderson, C. D., Khor, C. C., & Lai, P. S. (2024) · Biomedicines · doi:10.3390/biomedicines13010017 · Cited by 11 · see citing works

Comparative Assessment and High-Throughput Drug-Combination Profiling of TEAD-Palmitoylation Inhibitors in Hippo Pathway Deficient Mesothelioma

Evsen, L., Morris, P. J., Thomas, C. J., & Ceribelli, M. (2023) · Pharmaceuticals · doi:10.3390/ph16121635 · Cited by 10 · see citing works

MoA Studies of the TEAD P-Site Binding Ligand MSC-4106 and Its Optimization to TEAD1-Selective Amide M3686

Heinrich, T., Schwarz, D. F., Petersson, C., Gunera, J., Garg, S., Schneider, R., Keil, M., Grimmeisen, L., Lopez, A. U., Albers, L., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01949 · Cited by 10 · see citing works

Noncanonical role of Golgi-associated macrophage TAZ in chronic inflammation and tumorigenesis

Park, S. Y., Ju, S., Lee, J. H., Kim, H.-R., Sub, Y., Park, D. J., Park, S., Kwon, D., Kang, H.-G., Shin, J. E., et al. (2025) · Science Advances · doi:10.1126/sciadv.adq2395 · Cited by 10 · see citing works

UCHL3: a crucial deubiquitinase in DNA damage repair and tumor progression

Liu, J., Hu, S., Xiao, J., & Zhou, J. (2025) · Cancer Cell International · doi:10.1186/s12935-025-03884-x · Cited by 10 · see citing works

Pipeline to evaluate YAP-TEAD inhibitors indicates TEAD inhibition represses NF2 -mutant mesothelioma

Cunningham, R., Jia, S., Purohit, K. P., Nosková, M., Maniak, M. K., Lin, Y., Hui, N. S., Graham, R. E., Rossi, A. G., Cholewa-Waclaw, J., et al. (2025) · Life Science Alliance · doi:10.26508/lsa.202503241 · Cited by 11 · see citing works

Discovery of reversible and covalent TEAD 1 selective inhibitors MSC-1254 and MSC-5046 based on one scaffold

Carswell, E. L., Heinrich, T., Petersson, C., Gunera, J., Garg, S., Schwarz, D. F., Schlesiger, S., Fischer, F., Eichhorn, T., Calder, M., et al. (2024) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2024.129981 · Cited by 9 · see citing works

An updated patent review of TEAD modulators (2022–present)

Xu, D., Zhong, J., Zeng, Y., Zhang, X., Wang, C., Luo, C., & Xiong, H. (2025) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2025.2522747 · Cited by 9 · see citing works

PKN2 Is a Dependency of the Mesenchymal-like Cancer Cell State

Killarney, S. T., Mesa, G., Washart, R., Mayro, B., Dillon, K. A., Wardell, S. E., Newlin, M., Lu, M., Rmaileh, A. A., Liu, N., et al. (2024) · Cancer Discovery · doi:10.1158/2159-8290.cd-24-0928 · Cited by 8 · see citing works

Discovery of a Potent and Selective TEAD Degrader with Durable Degradation Activity

Cao, L., Yang, J., Liu, Y., Chen, X., Shi, Y., Zhao, Y., Zhang, Y., Chen, J., Li, B., Wen, W., et al. (2025) · Advanced Science · doi:10.1002/advs.202503277 · Cited by 8 · see citing works

Bidirectional relationship between cancer and depression: From shared mechanisms to integrated therapeutic strategies

Liu, Z., Wan, J., & Liu, S. (2026) · Cancer Letters · doi:10.1016/j.canlet.2026.218318 · Cited by 8 · see citing works

Role of the YAP/TAZ-TEAD Transcriptional Complex in the Metabolic Control of TRAIL Sensitivity by the Mevalonate Pathway in Cancer Cells

Yousfi, Y. E., Mora-Molina, R., López‐Rivas, A., & Yerbes, R. (2023) · Cells · doi:10.3390/cells12192370 · Cited by 8 · see citing works

Gene therapy for diffuse pleural mesotheliomas in preclinical models by concurrent expression of NF2 and SuperHippo

Zhu, R., Liu, X., Zhang, X., Zhong, Z., Qi, S., Jin, R., Gu, Y., Wang, Y., Chen, L., Chen, K., et al. (2024) · Cell Reports Medicine · doi:10.1016/j.xcrm.2024.101763 · Cited by 8 · see citing works

CDK9 Inhibition by Dinaciclib Is a Therapeutic Vulnerability in Epithelioid Hemangioendothelioma

Pobbati, A. V., Burtscher, A., Siva, N. R., Hallett, A., Romigh, T., Che, K., Zhao, B., Coker, J. A., Wang, N., Stauffer, S. R., et al. (2024) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-24-1097 · Cited by 7 · see citing works

Oncogenic YAP sensitizes cells to CHK1 inhibition via CDK4/6 driven G1 acceleration

Gertzmann, D., Presek, C., Mattes, A. L., Sänger, M., Zoller, M., Schülein‐Völk, C., Ade, C. P., Eilers, M., & Gaubatz, S. (2025) · EMBO Reports · doi:10.1038/s44319-025-00514-5 · Cited by 7 · see citing works

Synergistic effect of PAK and Hippo pathway inhibitor combination in NF2-deficient Schwannoma

Benton, D., Chow, H. Y., Karchugina, S., & Chernoff, J. (2024) · PLoS ONE · doi:10.1371/journal.pone.0305121 · Cited by 7 · see citing works

Transcription factor TCF7L1 targeting HSPB6 is involved in EMT and PI3K/AKT/mTOR pathways in bladder cancer

Li, Z., Li, J., Cao, Q., Shen, T., Wang, Y., He, H., & Tong, M. H. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.108024 · Cited by 7 · see citing works

The Hippo pathway as an antitumor target: time to focus on

Koroleva, O. A., Kurkin, A. V., & Shtil, A. A. (2024) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2024.2432395 · Cited by 7 · see citing works

ELK4 induced upregulation of HOMER3 promotes the proliferation and metastasis in glioma via Wnt/β-catenin/EMT signaling pathway

Wang, F., Zhou, H., Tian, Y., Wang, X., Huang, Y., Tu, Y., Li, L., & Zhen, H. (2025) · Biology Direct · doi:10.1186/s13062-025-00643-w · Cited by 6 · see citing works

Transcription factor TFAP2A drives the growth and metastasis and blocks ferroptosis of triple-negative breast cancer by activating PRAME transcription

Pei, B., Sun, H., & Xu, L.-Y. (2025) · Naunyn-Schmiedeberg's Archives of Pharmacology · doi:10.1007/s00210-025-04359-6 · Cited by 7 · see citing works

γδ T cell-stromal networks modulate matrix composition and vascularity in foreign body response

Ruta, A., Krishnan, K., Woo, J., Mejías, J. C., Gray-Gaillard, E. F., Maestas, D. R., Nguyen, H. H., Rindone, A. N., Cherry, C., Patatanian, M., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-71540-7 · Cited by 5 · see citing works

Single-cell multi-omics analysis reveals cancer regulatory elements of transcriptional programs and clinical implications

Tang, X., Zhang, Q., Shen, Z., Xiao, J., Li, M., Meng, X., Wang, C., Zhang, G., Liu, A., & Yin, Y. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-08060-7 · Cited by 5 · see citing works

Translating molecular mechanisms of epithelioid hemangioendothelioma to improve patient outcome

Beretta, A., Stacchiotti, S., Tam, Y. B., Jones, R. L., Giani, C., Zaffaroni, N., Huang, P. H., & Pasquali, S. (2025) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2025.105021 · Cited by 5 · see citing works

Discovery of Clinical Candidate IAG933, a Potent YAP-TEAD PPI Disrupter

Vögtle, M., Sellner, H., Chapeau, E. A., Furet, P., Salem, B., Douget, M. L., Bordas, V., Groell, J., Goff, A.-L. L., Rouzet, C., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c03009 · Cited by 5 · see citing works

NSUN2 promoted tumor growth and metastatic via m5C-regulation of YAP through ALYREF/YBX1 axis in NSCLC

Li, R., Jin, D., Shao, S., & Guo, J. (2026) · Cell Death and Disease · doi:10.1038/s41419-025-08353-x · Cited by 5 · see citing works

RHOA drivers take alternate routes in gastric cancer

Benton, D., & Chernoff, J. (2023) · Science Signaling · doi:10.1126/scisignal.adk9171 · Cited by 5 · see citing works

Regulation of Hippo–YAP signaling axis by Isoalantolactone suppresses tumor progression in cholangiocarcinoma

Kim, C.-L., Lim, S.-B., Kim, D. H., Sim, Y. E., Kang, L., Park, S. J., Kim, H., Roh, T. H., Mo, J., & Jeong, H.-S. (2024) · Translational Oncology · doi:10.1016/j.tranon.2024.101971 · Cited by 5 · see citing works

Identification of pyrazolo-piperidinone derivatives targeting YAP-TEAD interface 3 as anticancer agents through integrated virtual screening and mass spectrometry proteomics.

Scalvini, L., Tagliazucchi, L., Elisi, G. M., Zappaterra, D., Moschella, M. G., Fantini, S., Aiello, D., Guerrini, R., Albanese, V., Pacifico, S., et al. (2025) · European journal of medicinal chemistry · doi:10.1016/j.ejmech.2025.118056 · Cited by 5 · see citing works

TRIMming away colon cancer: TRIM21-mediated ubiquitination as an activator of the Hippo tumor suppressor pathway

Benton, D., & Chernoff, J. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.06.023 · Cited by 5 · see citing works

Novel Indazole Compounds as TEAD Inhibitors for Treating Cancer

Sabnis, R. W. (2023) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.3c00392 · Cited by 5 · see citing works

SARS-CoV-2 NSP13 interacts with TEAD to suppress Hippo-YAP signaling

Meng, F., Kim, J.-H., Tsai, C.-R., Steimle, J. D., Wang, J., Shi, Y., Li, R. G., Xie, B., Deshmukh, V., Liu, S., et al. (2025) · eLife · doi:10.7554/elife.100248.3 · Cited by 4 · see citing works

Covalent pan-TEAD inhibitors block YAP activity and demonstrate brain penetrance in a Hippo-dependent cancer model

Hagenbeek, T. J., Zbieg, J. R., Smith, R., Paul, S., Gerosa, L., Torrini, C., Guarnaccia, A. D., Ong, C. C., Lacap, J. A., Ning, M., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-74722-5 · Cited by 4 · see citing works

Discovery and biological evaluation of carborane-containing derivatives as TEAD auto palmitoylation inhibitors

Li, C., Zhang, Y., Zhang, Z., Zhang, Y., Song, Y., Wang, L., Yuan, C., Hao, G., Sun, N., Li, H., et al. (2025) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2025.130155 · Cited by 4 · see citing works

Mechanism study of serum extracellular nano-vesicles miR-412-3p targeting regulation of TEAD1 in promoting malignant biological behavior of sub-centimeter lung nodules

Deng, Y., Patel, N. D., Ding, S., & Zhang, H. (2024) · Cancer Biomarkers · doi:10.3233/cbm-240137 · Cited by 3 · see citing works

Hippo pathway effectors are associated with glioma patient survival, control cell proliferation and sterol metabolism through TEAD3

Masliantsev, K., Desette, A., Gonzalez, A., Garrouche, I., Noblanc, A., Soulard, M., Triquard, M., Milin, S., Wager, M., Karayan, L., et al. (2025) · Brain Pathology · doi:10.1111/bpa.70021 · Cited by 3 · see citing works

TFAP4/DLGAP5 promotes tumor progression and macrophage M2 polarization in prostate cancer by activating the JAK2/STAT3 signaling

Li, S., Dong, Q., Ren, W., Yi, S., Wang, Z., & Pan, L. (2025) · Experimental Cell Research · doi:10.1016/j.yexcr.2025.114753 · Cited by 3 · see citing works

PARP1-mediated PARylation of TEAD4 stabilizes the YAP1-TEAD4 complex and promotes growth and immune evasion in breast cancer cells

Guo, Y., Song, G., Zou, H., Lu, L., Dai, X., Sun, C., Huangen, C. H. E. N., Tong, T., Huang, M., Zhu, M., et al. (2025) · Science Signaling · doi:10.1126/scisignal.adx2532 · Cited by 3 · see citing works

FRA1 drives melanoma metastasis through an actionable transcriptional network

Xu, X., Jarajapu, V., Chadourne, M., Soto-Vargas, Z., Ochoa-Rios, S. L., Jasani, N., Wang, K., Mecozzi, N., Yao, J., Yu, X., et al. (2025) · Oncogene · doi:10.1038/s41388-025-03632-5 · Cited by 3 · see citing works

Expanding the toolbox to develop IAP-based degraders of TEAD transcription factors

Gupta, N., Trainor, N., Radwan, M., Nguyen, S., Duncan, L., Tang, A. X., Beveridge, J., Silke, N., Yousef, J. M., Bilgilier, C., et al. (2026) · Communications Chemistry · doi:10.1038/s42004-025-01871-x · Cited by 4 · see citing works

Discovery of Pan-TEAD Inhibitors That Disrupt YAP-TEAD Interaction as a Potential Therapy for Gastric Cancers and Mutant KRAS and EGFR Lung Cancers

Kumar, R., Thian, J., Toh, J. D. W., Mohideen, N. F., Sun, J., Kang, C., Low, S. M. C., Wee, S., Lim, Z., Gunaratne, J., et al. (2026) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5c00590 · Cited by 3 · see citing works

The Hippo Pathway Is Dysregulated in Cancer-Associated Fibroblasts in Anti–PD-L1–Resistant Cancer

Roels, J., Ghaedi, H., Kancherla, J., Yang, Y., Ganesan, R., Babu, P., Williams, K., Yao, X., Pradhan, R., Guan, X., et al. (2026) · Cancer Research · doi:10.1158/0008-5472.can-24-3954 · Cited by 3 · see citing works

EDNRA Forms a Positive Feedback Loop with the Hippo/YAP Axis to Drive Triple‐Negative Breast Cancer Progression

Hong, Z., Li, B., Xu, J., Lin, R., Pan, J., Fang, C., Zhang, B., Lau, L. Y., Aldridge, R. J., Whitmore, E. A., et al. (2026) · Advanced Science · doi:10.1002/advs.76784 · Cited by 3 · see citing works

Drug targets regulate systemic metabolism and provide new horizons to treat nonalcoholic steatohepatitis

Wang, Y., Yu, H., Cen, Z., Zhu, Y., & Wu, W. (2023) · Metabolism Open · doi:10.1016/j.metop.2023.100267 · Cited by 3 · see citing works

Key roles of ubiquitination in regulating critical regulators of cancer stem cell functionality

Guo, Q., Qin, H., Chen, Z., Zhang, W., Zheng, L., & Qin, T. (2024) · Genes & Diseases · doi:10.1016/j.gendis.2024.101311 · Cited by 3 · see citing works

The YAP1-MAML2 fusion drives tumorigenesis and sustains tumor growth

Ni, W., Yu, M., Yang, R., Li, J. W., Zhou, X., Calbay, O., Pi, L., Lu, J., Huang, S., & Wu, L. (2024) · Molecular Therapy Oncology · doi:10.1016/j.omton.2024.200900 · Cited by 3 · see citing works

An oncoembryology approach uncovers SoxC-driven regulation of colon development and cancerPreprint

Dalessi, T., Valenta, T., Moro, G., Brügger, M. D., Meijs, A., Szczerba, B. M., Brunner, T., Lampart, S., Nater, M., Platt, R. J., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.08.617191 · Cited by 3 · see citing works

Structural and functional basis of PU.1-BAF interaction enables targeting of lineage-specific transcription

Sadalge, D., Clasman, J. R., Topal, S., Musser, D., Von der Porten, L., Wu, S., Schultz, S. E., Austin, W., Huang, D., Gao, Y.-D., et al. (2025) · doi:10.1101/2025.08.01.667454 · Cited by 2 · see citing works

Phase II study of axitinib in patients with NF2-related schwannomatosis and progressive vestibular schwannomas

Garcia, M. R., Hagiwara, M., Yaffe, A., Mitchell, C., Akshintala, S., Nicolaides, T. P., Phadnis, S., Yohay, K. H., Feng, Y., Goldberg, J. D., et al. (2025) · Neuro-Oncology Advances · doi:10.1093/noajnl/vdaf083 · Cited by 2 · see citing works

Alexidine is a TAZ-specific small-molecule inhibitor that suppresses breast cancer invasion and metastasis

Ge, A., Niu, L., Rubino, R., Seaman, K., Song, X., Hao, Y., Klupt, K. A., Iaboni, N., Jia, Z., You, L., et al. (2025) · iScience · doi:10.1016/j.isci.2025.114116 · Cited by 2 · see citing works

CD155 reprograms glycolysis via the YAP/TEAD1-GLUT1 axis to promote lung adenocarcinoma progression and M2 macrophage polarization: a metabolic-immune target visualized by 18F-FDG PET/CT

Cheng, Z., Wang, S., Xu, S., Wang, Y., Diao, Y., Du, B., Li, X., & Li, Y. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-07551-7 · Cited by 2 · see citing works

CNS penetrant TEAD1,2,4 inhibitor MSC-4070 derived from phenotypic screening hit optimization

Heinrich, T., Petersson, C., Gunera, J., Gambardella, A., Schwarz, D., Garg, S., Schilke, H., Weitzel, T., Kolb, C., Anlauf, U., et al. (2026) · RSC Medicinal Chemistry · doi:10.1039/d5md00928f · Cited by 2 · see citing works

TEAD1::NCOA2 fusion driver in primary central nervous system malignancy: case report

Панферова, А. В., Сенченко, М. А., Zaytseva, M., Rasskazova, Y., Abasov, R. K., Tarakanova, A. V., Usman, N. Y., Papusha, L. I., & Druy, A. E. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02851-0 · Cited by 2 · see citing works

PPP1CA promotes hepatocellular carcinoma progression in a YAP1-dependent way

Liu, X., Xu, G., Luo, W., Wang, K., & Wang, F. (2025) · Cellular Signalling · doi:10.1016/j.cellsig.2025.111938 · Cited by 2 · see citing works

Current Model Systems for Investigating Epithelioid Haemangioendothelioma

Neil, E., & Kouskoff, V. (2023) · Cancers · doi:10.3390/cancers15113005 · Cited by 2 · see citing works

Novel Compounds as TEAD Inhibitors for Treating Cancer

Sabnis, R. W. (2023) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.3c00346 · Cited by 2 · see citing works

OTUD6A orchestrates complex modulation of TEAD4 ‐mediated transcriptional programs

Kim, H. J., Choi, Y.-S., Lee, Y., Hwangbo, M. H., & Kim, J. (2024) · FEBS Letters · doi:10.1002/1873-3468.14861 · Cited by 1 · see citing works

Decoy oligodeoxynucleotides targeting STATs in non-cancer gene therapy

Mahjoubin‐Tehran, M., Rezaei, S., Kesharwani, P., Karav, S., & Sahebkar, A. (2025) · Gene · doi:10.1016/j.gene.2025.149482 · Cited by 1 · see citing works

Integrative High-Throughput RNAi Screening Identifies BRSK1, STK32C and STK40 as Novel Activators of YAP/TAZ

Gill, M. K., Song, S., Christova, T. Y., & Attisano, L. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26167810 · Cited by 1 · see citing works

Hippo signaling as a therapeutic switch for T cell functions and tumor immunity

Fan, J., Riaz, F., & Riaz, F. (2026) · Molecular Immunology · doi:10.1016/j.molimm.2025.12.013 · Cited by 1 · see citing works

Subtype-Dependent Expression Patterns of Core Hippo Pathway Components in Thymic Epithelial Tumors (TETs): An RT-qPCR Study

Elm, L., Gerlitz, N., Neumann, J. H. L., & Levidou, G. (2026) · Biomedicines · doi:10.3390/biomedicines14020305 · Cited by 1 · see citing works

Targeting TEAD in cancer

Battina, R., Rahhal, R., Wellstein, A., Riegel, A. T., & Sharif, G. M. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1692512 · Cited by 15 · see citing works

Targeting the Hippo Pathway and Cancer through the TEAD Family of Transcription Factors

Holden, J. K., & Cunningham, C. N. (2018) · Cancers · doi:10.3390/cancers10030081 · Cited by 175 · see citing works

A chemical perspective on the modulation of TEAD transcriptional activities: Recent progress, challenges, and opportunities

Lou, J., Lu, Y., Cheng, J., Zhou, F., Yan, Z., Zhang, D., Meng, X., & Zhao, Y. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114684 · Cited by 39 · see citing works

Abstract 2474: Potent small molecule TEAD inhibitors targeting the Hippo pathway exhibit antiproliferation in vitro and anti-tumor effect in vivo

Amidon, B., Syed, S., Cavanaugh, J., Frosch, H., Natarajan, P., Ecsedy, J., McGovern, K., & Castro, A. C. (2020) · Cancer Research · doi:10.1158/1538-7445.am2020-2474

Abstract 4516: Inhibiting YAP activity in cancers by targeted degradation of TEAD

Chen, H., Gridnev, A., Schlamowitz, N. S., Zheng, G., & Misra, J. R. (2024) · Cancer Research · doi:10.1158/1538-7445.am2024-4516